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J Biol Chem, Vol. 273, Issue 37, 23805-23811, September 11, 1998
From the Departments of Medicine and Biochemistry, University of
Utah Health Science Center, Salt Lake City, Utah 84132
Mac1 from Saccharomyces cerevisiae
activates transcription of genes, including CTR1 in
copper-deficient cells. N-terminal fusions of Mac1 with the herpes
simplex VP16 activation domain were used to show that residues 1-159
in Mac1 constitute the minimal DNA binding domain. Mac1-(1-159)
purified from Escherichia coli contains two bound Zn(II)
ions. Electrophoretic mobility shift assays showed direct and specific
binding by Mac1-(1-159) to a DNA duplex containing the
copper-responsive element TTTGCTCA. The DNA binding affinity of
Mac1-(1-159) for a duplex containing a single promoter element or an
inverted repeat was 5 nM for the 1:1 complex. The
N-terminal 40-residue segment of Mac1 is homologous to the DNA binding
zinc module found in the copper-activated transcription factors Ace1
and Amt1. A MAC1 mutation yielding a Cys11
Mapping of the DNA Binding Domain of the Copper-responsive
Transcription Factor Mac1 from Saccharomyces
cerevisiae
Tyr substitution at the first candidate zinc ligand
position relative to Ace1 resulted in a loss of in vivo
function. Two TTTGCTCA promoter elements are necessary for efficient
Mac1-mediated transcriptional activation. The elements appear to
function synergistically. Increasing the number of elements yields more
than additive enhancements in CTR1 expression.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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